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-catalysts that accelerate the rates of chemical reactions in biological environments |
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-anything that can lower the activation energy without being consumed by the reaction |
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-necessary for life -genetic diseases (cystic fibrosis) -diagnostic tools (creatine kinase) -drugs that interact with enzymes (statins) -food processing and chemical industry -biological weapons |
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-MOST enzymes are proteins -usually make or break a covalent bond -highly selective -highly specific |
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-catalyzing only 1 reaction |
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-bind only 1 specific substrate |
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within the active site and participate in catalytic reactions and help hold substrate in place |
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non-covalent interactions |
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-electrostatic -h-bonds -van der waals -hydrophobic |
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molecules in a liquid will collide and bounce off one another |
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rate of enzyme-substrate contact depends on |
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movement and concentration of substrate |
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enzymes speed up reactions by selectively stabilizing the |
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-catalyze oxidation-reduction reaction -oxidation state of one or more atoms is altered -involves transfer of 1-2 electrons -95% of the time oxygen or hydrogen are added/removed -ex. disulfram |
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-catalyze transfer of molecular groups from a donor to an acceptor -ex. carboxyl,carbonyl,methyl,phsophoryl,acyl |
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-catalyze hydro lysis reactions -cleavage of bonds is done by addition of water -CO, CN, OP bonds usually -ex. Saquinavir (HIV enzyme inhibitor) |
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-catalyze the cleavage/formation of CC, CO, CN bonds by other means than hydrolysis/oxidation -almost always associated with double bonds -ex. Acetazolamide (Diamox) |
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-Diamox -carbonic anhydrase inhibitor -acute motion sickness -glaucoma -edema |
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-catalyze intramolecular rearrangement -isomerase-rearranges isomers (move atom) -mutase-intramolecular functional group (moving molecules) -ex. quinilone antibiotics(cirpofloxacin/moxifloxican) (DNA gyrase) |
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-catalyze covalent bond formation -require ATP |
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-additional non protein required for enzyme activity -metal ions -coenzymes |
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metal ions (essential ions) |
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-1/3 enzymes require -metal-activated enzymes -metalloenzymes |
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-metal is loosely bond (reversible) -usually alkali/alkaline earth metals -metal plays a role in substrate binding and enzyme structure -multiple metal binding sites on enzyme -ex. hexokinase |
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-metal is TIGHTLY bound-covalent -usually transition metals -metal plays a role in catalytic activity -usually one metal binding site |
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metal activated cofactors |
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-small ORGANIC molecules -possess reactive groups that are not found on amino acid side chains -can act as carriers for substrate molecules -necessary for enzyme activity but not true catalysts -chemically changed by reaction -must be regenerated before being used again |
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-classified based on binding strength (cosubstrates/prosthetic groups) -most are vitamins |
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-loosely bound -often transfer mobile metabolic groups or energy source among molecules -act as substrates -changed during the reaction,dissociates |
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-tightly bound -remain bound during and after reaction -changed during the reaction |
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NAD+ and NADP+ vitamin source |
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coenzyme A vitamin source |
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folate (folic acid,vit B9) |
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FMN and FAD vitamin source |
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